Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp.
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Bioscience journal (Online) |
Texto Completo: | https://seer.ufu.br/index.php/biosciencejournal/article/view/53865 |
Resumo: | Enzymes of the archaea living in extreme environments are resistant to the challenging conditions. Lipase is among the important enzymes used in the industry and agriculture. In this study, the extracellular lipase from extremely halophilic archaeon Halolamina sp. was characterized for the first time. Optimum temperature for the enzyme activity was determined as 70oC, optimum pH was 7.0, and the optimum salt concentration was 3.6 M. Additionally, more than 70% of the enzyme activity was remained between pH 3.0-10.0 for 48 h as well as incubation of the enzyme at 70oC for 30 min increased its activity for 44%, and no activity loss was observed after incubation at 80oC. Also, presence of the metals increased the enzyme activity up to 88%. The enzyme was highly resistant to the organic solvents acetone, methanol, and DMSO while strong inhibition was caused by n-butanol. Among the detergents, the enzyme kept its activity substantially in the presence of SDS; however, other detergents caused inhibition of the enzyme activity. This characterization study showed that the lipase from the haloarchaeon Halolamina sp. is highly stable at the wide ranges of temperature and pH values as well as in the presence of diverse inhibitors. This enzyme is promising to be used in biotechnological applications. |
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Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp.ArchaeabacteriaEnzyme StabilityHalolaminaLipase.Biological SciencesEnzymes of the archaea living in extreme environments are resistant to the challenging conditions. Lipase is among the important enzymes used in the industry and agriculture. In this study, the extracellular lipase from extremely halophilic archaeon Halolamina sp. was characterized for the first time. Optimum temperature for the enzyme activity was determined as 70oC, optimum pH was 7.0, and the optimum salt concentration was 3.6 M. Additionally, more than 70% of the enzyme activity was remained between pH 3.0-10.0 for 48 h as well as incubation of the enzyme at 70oC for 30 min increased its activity for 44%, and no activity loss was observed after incubation at 80oC. Also, presence of the metals increased the enzyme activity up to 88%. The enzyme was highly resistant to the organic solvents acetone, methanol, and DMSO while strong inhibition was caused by n-butanol. Among the detergents, the enzyme kept its activity substantially in the presence of SDS; however, other detergents caused inhibition of the enzyme activity. This characterization study showed that the lipase from the haloarchaeon Halolamina sp. is highly stable at the wide ranges of temperature and pH values as well as in the presence of diverse inhibitors. This enzyme is promising to be used in biotechnological applications.EDUFU2022-08-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://seer.ufu.br/index.php/biosciencejournal/article/view/5386510.14393/BJ-v38n0a2022-53865Bioscience Journal ; Vol. 38 (2022): Continuous Publication; e38039Bioscience Journal ; v. 38 (2022): Continuous Publication; e380391981-3163reponame:Bioscience journal (Online)instname:Universidade Federal de Uberlândia (UFU)instacron:UFUenghttps://seer.ufu.br/index.php/biosciencejournal/article/view/53865/34384Turkey; Contemporary Copyright (c) 2022 Sezer Okay, Şevki Adem, Aslıhan Kurt-Kizildoğanhttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessOkay, SezerAdem, ŞevkiAslıhan Kurt-Kizildoğan2022-08-08T16:09:33Zoai:ojs.www.seer.ufu.br:article/53865Revistahttps://seer.ufu.br/index.php/biosciencejournalPUBhttps://seer.ufu.br/index.php/biosciencejournal/oaibiosciencej@ufu.br||1981-31631516-3725opendoar:2022-08-08T16:09:33Bioscience journal (Online) - Universidade Federal de Uberlândia (UFU)false |
dc.title.none.fl_str_mv |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
title |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
spellingShingle |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. Okay, Sezer Archaeabacteria Enzyme Stability Halolamina Lipase. Biological Sciences |
title_short |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
title_full |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
title_fullStr |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
title_full_unstemmed |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
title_sort |
Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
author |
Okay, Sezer |
author_facet |
Okay, Sezer Adem, Şevki Aslıhan Kurt-Kizildoğan |
author_role |
author |
author2 |
Adem, Şevki Aslıhan Kurt-Kizildoğan |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Okay, Sezer Adem, Şevki Aslıhan Kurt-Kizildoğan |
dc.subject.por.fl_str_mv |
Archaeabacteria Enzyme Stability Halolamina Lipase. Biological Sciences |
topic |
Archaeabacteria Enzyme Stability Halolamina Lipase. Biological Sciences |
description |
Enzymes of the archaea living in extreme environments are resistant to the challenging conditions. Lipase is among the important enzymes used in the industry and agriculture. In this study, the extracellular lipase from extremely halophilic archaeon Halolamina sp. was characterized for the first time. Optimum temperature for the enzyme activity was determined as 70oC, optimum pH was 7.0, and the optimum salt concentration was 3.6 M. Additionally, more than 70% of the enzyme activity was remained between pH 3.0-10.0 for 48 h as well as incubation of the enzyme at 70oC for 30 min increased its activity for 44%, and no activity loss was observed after incubation at 80oC. Also, presence of the metals increased the enzyme activity up to 88%. The enzyme was highly resistant to the organic solvents acetone, methanol, and DMSO while strong inhibition was caused by n-butanol. Among the detergents, the enzyme kept its activity substantially in the presence of SDS; however, other detergents caused inhibition of the enzyme activity. This characterization study showed that the lipase from the haloarchaeon Halolamina sp. is highly stable at the wide ranges of temperature and pH values as well as in the presence of diverse inhibitors. This enzyme is promising to be used in biotechnological applications. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-08-05 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://seer.ufu.br/index.php/biosciencejournal/article/view/53865 10.14393/BJ-v38n0a2022-53865 |
url |
https://seer.ufu.br/index.php/biosciencejournal/article/view/53865 |
identifier_str_mv |
10.14393/BJ-v38n0a2022-53865 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
https://seer.ufu.br/index.php/biosciencejournal/article/view/53865/34384 |
dc.rights.driver.fl_str_mv |
Copyright (c) 2022 Sezer Okay, Şevki Adem, Aslıhan Kurt-Kizildoğan https://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Copyright (c) 2022 Sezer Okay, Şevki Adem, Aslıhan Kurt-Kizildoğan https://creativecommons.org/licenses/by/4.0 |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.coverage.none.fl_str_mv |
Turkey; Contemporary |
dc.publisher.none.fl_str_mv |
EDUFU |
publisher.none.fl_str_mv |
EDUFU |
dc.source.none.fl_str_mv |
Bioscience Journal ; Vol. 38 (2022): Continuous Publication; e38039 Bioscience Journal ; v. 38 (2022): Continuous Publication; e38039 1981-3163 reponame:Bioscience journal (Online) instname:Universidade Federal de Uberlândia (UFU) instacron:UFU |
instname_str |
Universidade Federal de Uberlândia (UFU) |
instacron_str |
UFU |
institution |
UFU |
reponame_str |
Bioscience journal (Online) |
collection |
Bioscience journal (Online) |
repository.name.fl_str_mv |
Bioscience journal (Online) - Universidade Federal de Uberlândia (UFU) |
repository.mail.fl_str_mv |
biosciencej@ufu.br|| |
_version_ |
1797069082497908736 |